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Self-Assembly of Highly Ordered Peptide Amphiphile Metalloporphyrin Arrays

Fry, H. Christopher, Garcia, Jamie M., Medina, Matthew J., Ricoy, Ulises M., Gosztola, David J., Nikiforov, Maxim P., Palmer, Liam C., Stupp, Samuel I.
Journal of the American Chemical Society 2012 v.134 no.36 pp. 14646-14649
absorption, atomic force microscopy, electron microscopy, histidine, protoporphyrin, zinc
Long fibers assembled from peptide amphiphiles capable of binding the metalloporphyrin zinc protoporphyrin IX ((PPIX)Zn) have been synthesized. Rational peptide design was employed to generate a peptide, c16-AHL₃K₃-CO₂H, capable of forming a β-sheet structure that propagates into larger fibrous structures. A porphyrin-binding site, a single histidine, was engineered into the peptide sequence in order to bind (PPIX)Zn to provide photophysical functionality. The resulting system indicates control from the molecular level to the macromolecular level with a high order of porphyrin organization. UV/visible and circular dichroism spectroscopies were employed to detail molecular organization, whereas electron microscopy and atomic force microscopy aided in macromolecular characterization. Preliminary picosecond transient absorption data are also reported. Reduced hemin, (PPIX)Feᴵᴵ, was also employed to highlight the material’s versatility and tunability.